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A4JG73 (A4JG73_BURVG) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A synthetase HAMAP-Rule MF_01123

Short name=AcCoA synthetase HAMAP-Rule MF_01123
Short name=Acs HAMAP-Rule MF_01123
EC=6.2.1.1 HAMAP-Rule MF_01123
Alternative name(s):
Acetate--CoA ligase HAMAP-Rule MF_01123
Acyl-activating enzyme HAMAP-Rule MF_01123
Gene names
Name:acsA HAMAP-Rule MF_01123
Ordered Locus Names:Bcep1808_2277 EMBL ABO55276.1
OrganismBurkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia (strain R1808)) [Complete proteome] [HAMAP] EMBL ABO55276.1
Taxonomic identifier269482 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity. HAMAP-Rule MF_01123

Catalytic activity

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA. HAMAP-Rule MF_01123

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01123

Post-translational modification

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity. HAMAP-Rule MF_01123

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family. HAMAP-Rule MF_01123

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region421 – 4266Substrate binding By similarity HAMAP-Rule MF_01123

Sites

Active site5301 By similarity HAMAP-Rule MF_01123
Metal binding5501Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5521Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Metal binding5551Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_01123
Binding site3171Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site3971Substrate; via nitrogen amide By similarity HAMAP-Rule MF_01123
Binding site5121Substrate By similarity HAMAP-Rule MF_01123
Binding site5281Substrate By similarity HAMAP-Rule MF_01123
Binding site5361Coenzyme A By similarity HAMAP-Rule MF_01123
Binding site5391Substrate By similarity HAMAP-Rule MF_01123
Binding site6001Coenzyme A By similarity HAMAP-Rule MF_01123

Amino acid modifications

Modified residue6251N6-acetyllysine By similarity HAMAP-Rule MF_01123

Sequences

Sequence LengthMass (Da)Tools
A4JG73 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 175CF239E0DB3C32

FASTA66072,019
        10         20         30         40         50         60 
MSAIESVLHE TRQFAPPAAL EKTATISGMP AYRALVAEAE QDYEGFWARL ARENLSWHKP 

        70         80         90        100        110        120 
FTKVLDESNA PFCTWFDDGE LNASYNCLDR HVEAGNGQRV AVIFEADDGT VTRVTYAELL 

       130        140        150        160        170        180 
ARVSRFANAL KKRGIGKGDR VVIYIPMSIE GIVAMQACAR IGATHSVVFG GFSAKSLNER 

       190        200        210        220        230        240 
LVDVGAVALI TADEQARGGK TLPLKSIADE AIAMGGCDAV KSVIVYRRTG GKIDWHAGRD 

       250        260        270        280        290        300 
LWMHELADAE SDHCPPEWVG AEHPLFILYT SGSTGKPKGV QHSTGGYLLW AAQTMKWTFD 

       310        320        330        340        350        360 
WKPDDVFWCT ADIGWVTGHT YITYGPLACG GTQVVFEGVP TYPDAGRFWK MIADHKVSVF 

       370        380        390        400        410        420 
YTAPTAIRSL IKAADADDKV HPKSYDLSSL RIIGTVGEPI NPDAWMWYHK HVGGERCPIV 

       430        440        450        460        470        480 
DTWWQTETGG HMITPLPGAT PTVPGSCTLP LPGIMAAVVD ETGQDVPNGQ GGILVVKRPW 

       490        500        510        520        530        540 
PSMIRTIWGD PERFKKSYYP EELGGGLYLA GDGTVRDKDT GYFTIMGRID DVLNVSGHRL 

       550        560        570        580        590        600 
GTMEIESALV SHELVAEAAV VGRPDDTTGE AVVAFVVLKR SRPEGDEAAA LAKALRDWVG 

       610        620        630        640        650        660 
KQIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEAI TQDTSTLENP AILEQLTEVR 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G4 / LMG 22486.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000614 Genomic DNA. Translation: ABO55276.1.
RefSeqYP_001120111.1. NC_009256.1.

3D structure databases

ProteinModelPortalA4JG73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269482.Bcep1808_2277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO55276; ABO55276; Bcep1808_2277.
GeneID4954012.
KEGGbvi:Bcep1808_2277.
PATRIC19323128. VBIBurVie89221_6515.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0365.
HOGENOMHOG000229981.
KOK01895.
OMAAWIWYRD.
OrthoDBEOG68WR2H.

Enzyme and pathway databases

BioCycBVIE269482:GJNA-2339-MONOMER.

Family and domain databases

HAMAPMF_01123. Ac_CoA_synth.
InterProIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA4JG73_BURVG
AccessionPrimary (citable) accession number: A4JG73
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: June 11, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)